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Volumn 79, Issue 3, 2011, Pages 1166-1175

Destabilization of YopE by the ubiquitin-proteasome pathway fine-tunes yop delivery into host cells and facilitates systemic spread of Yersinia enterocolitica in host lymphoid tissue

Author keywords

[No Author keywords available]

Indexed keywords

LYSINE; OUTER MEMBRANE PROTEIN; POLYUBIQUITIN; PROTEASOME; UBIQUITIN; UNCLASSIFIED DRUG; YERSINIA OUTER PROTEIN E; YERSINIA OUTER PROTEIN H; YERSINIA OUTER PROTEIN P;

EID: 79952310045     PISSN: 00199567     EISSN: 10985522     Source Type: Journal    
DOI: 10.1128/IAI.00694-10     Document Type: Article
Times cited : (18)

References (41)
  • 1
  • 2
    • 39849084503 scopus 로고    scopus 로고
    • Regulation of Yersinia Yop-effector delivery by translocated YopE
    • Aili, M., et al. 2008. Regulation of Yersinia Yop-effector delivery by translocated YopE. Int. J. Med. Microbiol. 298:183-192.
    • (2008) Int. J. Med. Microbiol. , vol.298 , pp. 183-192
    • Aili, M.1
  • 3
    • 33646358945 scopus 로고    scopus 로고
    • Functional analysis of the YopE GTPase-activating protein (GAP) activity of Yersinia pseudotuberculosis
    • Aili, M., E. L. Isaksson, B. Hallberg, H. Wolf-Watz, and R. Rosqvist. 2006. Functional analysis of the YopE GTPase-activating protein (GAP) activity of Yersinia pseudotuberculosis. Cell. Microbiol. 8:1020-1033.
    • (2006) Cell. Microbiol. , vol.8 , pp. 1020-1033
    • Aili, M.1    Isaksson, E.L.2    Hallberg, B.3    Wolf-Watz, H.4    Rosqvist, R.5
  • 4
    • 33846574355 scopus 로고    scopus 로고
    • Exploitation of eukaryotic ubiquitin signaling pathways by effectors translocated by bacterial type III and type IV secretion systems
    • Angot, A., A. Vergunst, S. Genin, and N. Peeters. 2007. Exploitation of eukaryotic ubiquitin signaling pathways by effectors translocated by bacterial type III and type IV secretion systems. PLoS Pathog. 3:e3.
    • (2007) PLoS Pathog. , vol.3
    • Angot, A.1    Vergunst, A.2    Genin, S.3    Peeters, N.4
  • 5
    • 33846783290 scopus 로고    scopus 로고
    • The ubiquitin ligase Cbl-b limits Pseudomonas aeruginosa exotoxin T-mediated virulence
    • Balachandran, P., et al. 2007. The ubiquitin ligase Cbl-b limits Pseudomonas aeruginosa exotoxin T-mediated virulence. J. Clin. Invest. 117:419-427.
    • (2007) J. Clin. Invest. , vol.117 , pp. 419-427
    • Balachandran, P.1
  • 6
    • 0032456889 scopus 로고    scopus 로고
    • Heterogeneity of the Yersinia YopM protein
    • Boland, A., S. Havaux, and G. R. Cornelis. 1998. Heterogeneity of the Yersinia YopM protein. Microb. Pathog. 25:343-348.
    • (1998) Microb. Pathog. , vol.25 , pp. 343-348
    • Boland, A.1    Havaux, S.2    Cornelis, G.R.3
  • 7
    • 44949187452 scopus 로고    scopus 로고
    • Reduced secretion of YopJ by Yersinia limits in vivo cell death but enhances bacterial virulence
    • Brodsky, I. E., and R. Medzhitov. 2008. Reduced secretion of YopJ by Yersinia limits in vivo cell death but enhances bacterial virulence. PLoS Pathog. 4:e1000067.
    • (2008) PLoS Pathog. , vol.4
    • Brodsky, I.E.1    Medzhitov, R.2
  • 8
    • 0015719054 scopus 로고
    • New strain of Yersinia enterocolitica pathogenic for rodents
    • Carter, P. B., C. F. Varga, and E. E. Keet. 1973. New strain of Yersinia enterocolitica pathogenic for rodents. Appl. Microbiol. 26:1016-1018.
    • (1973) Appl. Microbiol. , vol.26 , pp. 1016-1018
    • Carter, P.B.1    Varga, C.F.2    Keet, E.E.3
  • 9
    • 77950863509 scopus 로고    scopus 로고
    • Cytosol as battleground: Ubiquitin as a weapon for both host and pathogen
    • Collins, C. A., and E. J. Brown. Cytosol as battleground: ubiquitin as a weapon for both host and pathogen. Trends Cell Biol. 20:205-213.
    • Trends Cell Biol. , vol.20 , pp. 205-213
    • Collins, C.A.1    Brown, E.J.2
  • 10
    • 0034612342 scopus 로고    scopus 로고
    • One-step inactivation of chromosomal genes in Escherichia coli K-12 using PCR products
    • Datsenko, K. A., and B. L. Wanner. 2000. One-step inactivation of chromosomal genes in Escherichia coli K-12 using PCR products. Proc. Natl. Acad. Sci. U. S. A. 97:6640-6645.
    • (2000) Proc. Natl. Acad. Sci. U. S. A. , vol.97 , pp. 6640-6645
    • Datsenko, K.A.1    Wanner, B.L.2
  • 11
    • 0036081145 scopus 로고    scopus 로고
    • Effect of low- and high-virulence Yersinia enterocolitica strains on the inflammatory response of human umbilical vein endothelial cells
    • Denecker, G., et al. 2002. Effect of low- and high-virulence Yersinia enterocolitica strains on the inflammatory response of human umbilical vein endothelial cells. Infect. Immun. 70:3510-3520.
    • (2002) Infect. Immun. , vol.70 , pp. 3510-3520
    • Denecker, G.1
  • 12
    • 0141867599 scopus 로고    scopus 로고
    • DNA sequence and analysis of the pYVa127/90 virulence plasmid of Yersinia enterocolitica strain A127/90
    • Foultier, B., and G. R. Cornelis. 2003. DNA sequence and analysis of the pYVa127/90 virulence plasmid of Yersinia enterocolitica strain A127/90. Res. Microbiol. 154:553-557.
    • (2003) Res. Microbiol. , vol.154 , pp. 553-557
    • Foultier, B.1    Cornelis, G.R.2
  • 13
    • 67649400561 scopus 로고    scopus 로고
    • Common themes in the design and function of bacterial effectors
    • Galan, J. E. 2009. Common themes in the design and function of bacterial effectors. Cell Host Microbe 5:571-579.
    • (2009) Cell Host Microbe , vol.5 , pp. 571-579
    • Galan, J.E.1
  • 14
    • 0020555355 scopus 로고
    • Construction of a mobilizable Yersinia enterocolitica virulence plasmid
    • Heesemann, J., and R. Laufs. 1983. Construction of a mobilizable Yersinia enterocolitica virulence plasmid. J. Bacteriol. 155:761-767. (Pubitemid 13048114)
    • (1983) Journal of Bacteriology , vol.155 , Issue.2 , pp. 761-767
    • Heesemann, J.1    Laufs, R.2
  • 15
    • 34548481798 scopus 로고    scopus 로고
    • Serogroup-related escape of Yersinia enterocolitica YopE from degradation by the ubiquitin-proteasome pathway
    • Hentschke, M., K. Trulzsch, J. Heesemann, M. Aepfelbacher, and K. Ruckdeschel. 2007. Serogroup-related escape of Yersinia enterocolitica YopE from degradation by the ubiquitin-proteasome pathway. Infect. Immun. 75: 4423-4431.
    • (2007) Infect. Immun. , vol.75 , pp. 4423-4431
    • Hentschke, M.1    Trulzsch, K.2    Heesemann, J.3    Aepfelbacher, M.4    Ruckdeschel, K.5
  • 16
    • 75249101443 scopus 로고    scopus 로고
    • Hijacking the host ubiquitin pathway: Structural strategies of bacterial E3 ubiquitin ligases
    • Hicks, S. W., and J. E. Galan. Hijacking the host ubiquitin pathway: structural strategies of bacterial E3 ubiquitin ligases. Curr. Opin. Microbiol. 13:41-46.
    • Curr. Opin. Microbiol. , vol.13 , pp. 41-46
    • Hicks, S.W.1    Galan, J.E.2
  • 17
    • 33646596541 scopus 로고    scopus 로고
    • Application of comparative phylogenomics to study the evolution of Yersinia enterocolitica and to identify genetic differences relating to pathogenicity
    • DOI 10.1128/JB.188.10.3645-3653.2006
    • Howard, S. L., et al. 2006. Application of comparative phylogenomics to study the evolution of Yersinia enterocolitica and to identify genetic differences relating to pathogenicity. J. Bacteriol. 188:3645-3653. (Pubitemid 43726228)
    • (2006) Journal of Bacteriology , vol.188 , Issue.10 , pp. 3645-3653
    • Howard, S.L.1    Gaunt, M.W.2    Hinds, J.3    Witney, A.A.4    Stabler, R.5    Wren, B.W.6
  • 18
    • 70350433001 scopus 로고    scopus 로고
    • The membrane localization domain is required for intracellular localization and autoregulation of YopE in Yersinia pseudotuberculosis
    • Isaksson, E. L., et al. 2009. The membrane localization domain is required for intracellular localization and autoregulation of YopE in Yersinia pseudotuberculosis. Infect. Immun. 77:4740-4749.
    • (2009) Infect. Immun. , vol.77 , pp. 4740-4749
    • Isaksson, E.L.1
  • 19
    • 0344413859 scopus 로고    scopus 로고
    • Temporal regulation of Salmonella virulence effector function by proteasome-dependent protein degradation
    • Kubori, T., and J. E. Galan. 2003. Temporal regulation of Salmonella virulence effector function by proteasome-dependent protein degradation. Cell 115:333-342.
    • (2003) Cell , vol.115 , pp. 333-342
    • Kubori, T.1    Galan, J.E.2
  • 20
    • 0031970595 scopus 로고    scopus 로고
    • Targeting of Yersinia Yop proteins into the cytosol of HeLa cells: One-step translocation of YopE across bacterial and eukaryotic membranes is dependent on SycE chaperone
    • Lee, V. T., D. M. Anderson, and O. Schneewind. 1998. Targeting of Yersinia Yop proteins into the cytosol of HeLa cells: one-step translocation of YopE across bacterial and eukaryotic membranes is dependent on SycE chaperone. Mol. Microbiol. 28:593-601.
    • (1998) Mol. Microbiol. , vol.28 , pp. 593-601
    • Lee, V.T.1    Anderson, D.M.2    Schneewind, O.3
  • 21
    • 38949091134 scopus 로고    scopus 로고
    • Yersinia controls type III effector delivery into host cells by modulating Rho activity
    • Mejia, E., J. B. Bliska, and G. I. Viboud. 2008. Yersinia controls type III effector delivery into host cells by modulating Rho activity. PLoS Pathog. 4:e3.
    • (2008) PLoS Pathog. , vol.4
    • Mejia, E.1    Bliska, J.B.2    Viboud, G.I.3
  • 23
    • 64249106114 scopus 로고    scopus 로고
    • Diversification of a Salmonella virulence protein function by ubiquitin-dependent differential localization
    • Patel, J. C., K. Hueffer, T. T. Lam, and J. E. Galan. 2009. Diversification of a Salmonella virulence protein function by ubiquitin-dependent differential localization. Cell 137:283-294.
    • (2009) Cell , vol.137 , pp. 283-294
    • Patel, J.C.1    Hueffer, K.2    Lam, T.T.3    Galan, J.E.4
  • 24
  • 25
    • 0035253695 scopus 로고    scopus 로고
    • Yersinia outer protein P of Yersinia enterocolitica simultaneously blocks the nuclear factor-kappaB pathway and exploits lipopolysaccharide signaling to trigger apoptosis in macrophages
    • Ruckdeschel, K., et al. 2001. Yersinia outer protein P of Yersinia enterocolitica simultaneously blocks the nuclear factor-kappa B pathway and exploits lipopolysaccharide signaling to trigger apoptosis in macrophages. J. Immunol. 166:1823-1831. (Pubitemid 32114668)
    • (2001) Journal of Immunology , vol.166 , Issue.3 , pp. 1823-1831
    • Ruckdeschel, K.1    Mannel, O.2    Richter, K.3    Jacobi, C.A.4    Trulzsch, K.5    Rouot, B.6    Heesemann, J.7
  • 26
    • 33646486083 scopus 로고    scopus 로고
    • The proteasome pathway destabilizes Yersinia outer protein e and represses its antihost cell activities
    • Ruckdeschel, K., et al. 2006. The proteasome pathway destabilizes Yersinia outer protein E and represses its antihost cell activities. J. Immunol. 176: 6093-6102.
    • (2006) J. Immunol. , vol.176 , pp. 6093-6102
    • Ruckdeschel, K.1
  • 27
    • 0035190339 scopus 로고    scopus 로고
    • Arginine-143 of Yersinia enterocolitica YopP crucially determines isotype-related NF-κB suppression and apoptosis induction in macrophages
    • Ruckdeschel, K., K. Richter, O. Mannel, and J. Heesemann. 2001. Arginine-143 of Yersinia enterocolitica YopP crucially determines isotype-related NF-κB suppression and apoptosis induction in macrophages. Infect. Immun. 69:7652-7662.
    • (2001) Infect. Immun. , vol.69 , pp. 7652-7662
    • Ruckdeschel, K.1    Richter, K.2    Mannel, O.3    Heesemann, J.4
  • 28
    • 0030041090 scopus 로고    scopus 로고
    • Differential contribution of Yersinia enterocolitica virulence factors to evasion of microbicidal action of neutrophils
    • Ruckdeschel, K., A. Roggenkamp, S. Schubert, and J. Heesemann. 1996. Differential contribution of Yersinia enterocolitica virulence factors to evasion of microbicidal action of neutrophils. Infect. Immun. 64:724-733.
    • (1996) Infect. Immun. , vol.64 , pp. 724-733
    • Ruckdeschel, K.1    Roggenkamp, A.2    Schubert, S.3    Heesemann, J.4
  • 29
    • 33947714944 scopus 로고    scopus 로고
    • Bacterial interference of ubiquitination and deubiquitination
    • Rytkonen, A., and D. W. Holden. 2007. Bacterial interference of ubiquitination and deubiquitination. Cell Host Microbe 1:13-22.
    • (2007) Cell Host Microbe , vol.1 , pp. 13-22
    • Rytkonen, A.1    Holden, D.W.2
  • 30
    • 33644819006 scopus 로고    scopus 로고
    • Phosphorylation, ubiquitination and degradation of listeriolysin O in mammalian cells: Role of the PEST-like sequence
    • Schnupf, P., D. A. Portnoy, and A. L. Decatur. 2006. Phosphorylation, ubiquitination and degradation of listeriolysin O in mammalian cells: role of the PEST-like sequence. Cell Microbiol. 8:353-364.
    • (2006) Cell Microbiol. , vol.8 , pp. 353-364
    • Schnupf, P.1    Portnoy, D.A.2    Decatur, A.L.3
  • 31
    • 77951919509 scopus 로고    scopus 로고
    • Degradation of ubiquitin: The fate of the cellular reaper
    • Shabek, N., and A. Ciechanover. Degradation of ubiquitin: the fate of the cellular reaper. Cell Cycle 9:523-530.
    • Cell Cycle , vol.9 , pp. 523-530
    • Shabek, N.1    Ciechanover, A.2
  • 32
    • 0034971253 scopus 로고    scopus 로고
    • Complete DNA sequence of Yersinia enterocolitica serotype 0:8 low-calcium-response plasmid reveals a new virulence plasmid-associated replicon
    • Snellings, N. J., M. Popek, and L. E. Lindler. 2001. Complete DNA sequence of Yersinia enterocolitica serotype 0:8 low-calcium-response plasmid reveals a new virulence plasmid-associated replicon. Infect. Immun. 69:4627-4638.
    • (2001) Infect. Immun. , vol.69 , pp. 4627-4638
    • Snellings, N.J.1    Popek, M.2    Lindler, L.E.3
  • 34
    • 4544339989 scopus 로고    scopus 로고
    • Contribution of the major secreted yops of Yersinia enterocolitica O:8 to pathogenicity in the mouse infection model
    • Trulzsch, K., T. Sporleder, E. I. Igwe, H. Russmann, and J. Heesemann. 2004. Contribution of the major secreted yops of Yersinia enterocolitica O:8 to pathogenicity in the mouse infection model. Infect. Immun. 72:5227-5234.
    • (2004) Infect. Immun. , vol.72 , pp. 5227-5234
    • Trulzsch, K.1    Sporleder, T.2    Igwe, E.I.3    Russmann, H.4    Heesemann, J.5
  • 35
    • 0035477848 scopus 로고    scopus 로고
    • A bacterial type III secretion system inhibits actin polymerization to prevent pore formation in host cell membranes
    • Viboud, G. I., and J. B. Bliska. 2001. A bacterial type III secretion system inhibits actin polymerization to prevent pore formation in host cell membranes. EMBO J. 20:5373-5382.
    • (2001) EMBO J. , vol.20 , pp. 5373-5382
    • Viboud, G.I.1    Bliska, J.B.2
  • 36
    • 25444476788 scopus 로고    scopus 로고
    • Yersinia outer proteins: Role in modulation of host cell signaling responses and pathogenesis
    • Viboud, G. I., and J. B. Bliska. 2005. Yersinia outer proteins: role in modulation of host cell signaling responses and pathogenesis. Annu. Rev. Microbiol. 59:69-89.
    • (2005) Annu. Rev. Microbiol. , vol.59 , pp. 69-89
    • Viboud, G.I.1    Bliska, J.B.2
  • 37
    • 33746930289 scopus 로고    scopus 로고
    • Comparison of YopE and YopT activities in counteracting host signalling responses to Yersinia pseudotuberculosis infection
    • Viboud, G. I., E. Mejia, and J. B. Bliska. 2006. Comparison of YopE and YopT activities in counteracting host signalling responses to Yersinia pseudotuberculosis infection. Cell. Microbiol. 8:1504-1515.
    • (2006) Cell. Microbiol. , vol.8 , pp. 1504-1515
    • Viboud, G.I.1    Mejia, E.2    Bliska, J.B.3
  • 38
    • 20544472265 scopus 로고    scopus 로고
    • Molecular heterogeneity in Yersinia enterocolitica and 'Y. enterocolitica-like' speciesi-implications for epidemiology, typing and taxonomy
    • Virdi, J. S., and P. Sachdeva. 2005. Molecular heterogeneity in Yersinia enterocolitica and 'Y. enterocolitica-like' speciesi-implications for epidemiology, typing and taxonomy. FEMS Immunol. Med. Microbiol. 45:1-10.
    • (2005) FEMS Immunol. Med. Microbiol. , vol.45 , pp. 1-10
    • Virdi, J.S.1    Sachdeva, P.2
  • 39
    • 1342292545 scopus 로고    scopus 로고
    • The yersiniae - A model genus to study the rapid evolution of bacterial pathogens
    • Wren, B. W. 2003. The yersiniae - a model genus to study the rapid evolution of bacterial pathogens. Nat. Rev. Microbiol. 1:55-64.
    • (2003) Nat. Rev. Microbiol. , vol.1 , pp. 55-64
    • Wren, B.W.1
  • 40
    • 33744912761 scopus 로고    scopus 로고
    • Interaction of Yersinia pestis with macrophages: Limitations in YopJ-dependent apoptosis
    • Zauberman, A., et al. 2006. Interaction of Yersinia pestis with macrophages: limitations in YopJ-dependent apoptosis. Infect. Immun. 74:3239-3250.
    • (2006) Infect. Immun. , vol.74 , pp. 3239-3250
    • Zauberman, A.1
  • 41
    • 67650149415 scopus 로고    scopus 로고
    • Yersinia pestis endowed with increased cytotoxicity is avirulent in a bubonic plague model and induces rapid protection against pneumonic plague
    • Zauberman, A., et al. 2009. Yersinia pestis endowed with increased cytotoxicity is avirulent in a bubonic plague model and induces rapid protection against pneumonic plague. PLoS One 4:e5938.
    • (2009) PLoS One , vol.4
    • Zauberman, A.1


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